Ge Healthcare Bio-sciences Ab

Ge Healthcare Bioprocess R&d Ab

Cytiva Bioprocess R&d Ab

Amersham Biosciences Ab

Other

Puridify Ltd.

Jean-Luc Maloisel

Bo-Lennart Johansson

Gunnar Glad

Hans J Johansson

Nicolas Thevenin

Nils Norrman

Ronnie Palmgren

Annika Forss

Makonnen Belew

Bjorn Noren

Carina Engstrand

Ola Lind

Lars C Andersson

Tobias Soderman

Jan Bergstrom

Helena Skoglar

Karolina Busson

Gustav Jose Rodrigo

Martin Hall

Mattias Algotsson

Eggert Brekkan

Lee Hedemyr

Virendra Kumbhar

Robert Scott Youngquist

Andreas Axen

Enrique Napoleon Carredano

Karol Lacki

Shirley I Miekka

Tobias Söderman

Marc Hummersone

Anna Grönberg

Andreas Axén

William H Drohan

John Clachan

Ingrid Drevin

Anders Ljunglof

Ida Eklind

Thomas Woods Keough

Tesfai Gebru

Jafar Saidzadeh

Herbert Baumann

Jan Gustavsson

Mikael Andersson

Maria Liminga

Tania Ahmad

Ulrika Carlsson

Anders Ljunglöf

Anne Catharina Bergh

Helena Lindgren

Ake Stenholm

Maria Holm

Asa Ek

Jimmy Hedin Dahlström

Sara Häggblad Sahlberg

Ulf Tedebark

Tobias E SÖDERMAN

Jon Lundqvist

Bjorn NORÉN

The present invention relates to the field of chromatography. More closely, the invention relates to a chromatographic method for purification of proteins, such as Factor VIII, von Willebrand factor and Factor IX. The chromatographic method is performed on a matrix comprising an inner porous core and outer porous lid surrounding said core.

Chromatographic methods for purification of proteins from plasma

The invention discloses a separation matrix which comprises a plurality of separation ligands, defined by the formula R-L-N(R)-L-R, immobilized on a support, wherein Ris a five- or six-membered, substituted or non-substituted ring structure or a hydroxyethyl or hydroxypropyl group; Lis either a methylene group or a covalent bond; Ris a five- or six-membered, substituted or non-substituted ring structure; Lis either a methylene group or a covalent bond; Ris a methyl group; and wherein if Ris a hydroxyethyl group and Lis a covalent bond, Ris a substituted aromatic ring structure or a substituted or non-substituted aliphatic ring structure.

Multimodal anion exchange matrices

The present invention relates to the field of chromatography. More closely, the invention relates to a chromatographic method for purification of plasmaproteins, such as Factor VIII, von Willebrand factor and Factor IX. The chromatographic method is performed on a matrix comprising an inner porous core and outer porous lid surrounding said core.

The present invention is within the field of chromatography. More precisely, it relates to a novel chromatography medium, namely a hydrophobic medium provided with different lids excluding molecules over a certain size due to the porosity of the hydrophobic medium and/or the porosity of the lid. The invention also relates to use of the separation medium for purification of large molecules, which do not enter the separation medium, as well as small molecules, which enter the separation medium and are eluted from there.

Chromatography medium

The invention discloses a separation matrix for purification of biological particles, comprising a plurality of particles having a porous core entity and a porous shell entity covering the core entity, wherein the core entity comprises at least 50 micromole/ml primary amines present on covalently attached ligands displaying at least two primary amines per ligand and the shell entity comprises less than 20 micromole/ml primary amines The invention further discloses a method of purifying biological particles and a method of manufacturing a separation matrix.

Separation matrices for purification of biological particles

The present invention relates to a method for removal of large contaminants, such as virus, in a chromatographic process for purification of a target molecule, preferably monoclonal antibodies, mAbs, by using a specifically designed chromatographic bead having a thin outer layer and a core functionalized with a ligand adsorbing the mAbs or parts thereof.

Chromatography method

The invention discloses a separation matrix for purification of biomacromolecules, comprising a plurality of particles () having a core region () and a shell region (), wherein: a) said shell region is accessible to a target biomacromolecule; b) said core region is less accessible to the target biomacromolecule than the shell region; and c) the core region comprises a grafted polymer comprising residues of at least one polymerizable monomer.

Chromatography matrix

The invention discloses a separation matrix which comprises a plurality of separation ligands, defined by the formula R-L-N(R)-L-R, immobilized on a support, wherein Ris a five- or six-membered, substituted or non-substituted ring structure or a hydroxyethyl or hydroxypropyl group; Lis either a methylene group or a covalent bond; Ris a five-or six-membered, substituted or non-substituted ring structure; Lis either a methylene group or a covalent bond; Ris a methyl group; and wherein if Ris a hydroxyethyl group and Lis a covalent bond, Ris a substituted aromatic ring structure or a substituted or non-substituted aliphatic ring structure.

The present invention relates to a chromatography ligand defined by the following formula R&#x2014;R&#x2014;N(R)&#x2014;R&#x2014;Rwherein Ris a substituted or non-substituted phenyl group; Ris a hydrocarbon chain comprising 0-4 carbon atoms; Ris a hydrocarbon chain comprising 1-3 carbon atoms; Ris a hydrocarbon chain comprising 1-5 carbon atoms; and Ris OH or H. The invention also comprises a separation matrix, comprising the described ligands coupled to a porous support, such as particles or a membrane. The ligand and matrix according to the invention is useful for purification of biomolecules or organic compounds, such as proteins, polypeptides, DNA etc. An advantageous use according to the invention is the purification of antibodies.

Chromatography ligand

The present invention relates to dimeric pentadentate chelators with exceptionally strong binding of metal ions, for detection, immobilization and purification of biomolecules. Dimeric chelators offer a cooperativity of binding of two adjacent immobilized metal ions simultaneously to a histidine-tagged biomolecule, which gives advantageous properties regarding strength of binding compared to a corresponding monomer chelator. In addition, a dimer increases the selectivity (ease of separation) against non-tagged biomolecules with low metal-ion affinity.

Chelator and use thereof

The invention discloses a separation matrix with a porous solid support and a plurality of polyvinylpyrrolidone (PVP) polymer chains covalently attached to the solid support. The polyvinylpyrrolidone polymer chains are either vinylpyrrolidone homopolymer chains or copolymer chains which comprise at least 70 mol % vinylpyrrolidone monomer residues and less than 2 mol % negatively charged monomer residues.

Stabilization of fermented beverages

The present invention relates to dimeric pentadentate chelators with exceptionally strong binding of metal ions, for detection, immobilization and purification of biomolecules. Dimeric chelators offer a cooperativity of binding of two adjacent immobilized metal ions simultaneously to a histidine-tagged biomolecule, which gives advantageous properties regarding strength of binding compared to a corresponding monomer chelator. In addition, a dimer increases the selectivity (ease of separation) against non-tagged biomolecules with low metal-ion affinity. The dimeric pentadentate chelator according to the invention has the following general formula:  

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Uppsala, Sweden

Jean-Luc Maloisel